BRENDA - Enzyme Database

Investigation of interaction between enolase and phosphoglycerate mutase using molecular dynamics simulation

Hakobyan, D.; Nazaryan, K.; J. Biomol. Struct. Dyn. 23, 625-633 (2006)

Data extracted from this reference:

Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
4.2.1.11
2-phospho-D-glycerate
Saccharomyces cerevisiae
-
phosphoenolpyruvate + H2O
-
-
r
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
4.2.1.11
Saccharomyces cerevisiae
P00924
-
-
5.4.2.11
Saccharomyces cerevisiae
-
-
-
Specific Activity [micromol/min/mg]
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
4.2.1.11
additional information
-
binding affinity between enolase and phosphoglycerate mutase confirmed by interaction energies and conformation changes, 10 A resolution and three orientations positioning enolase towards to phosphoglycerate mutase tested in presence of 150 mM NaCl
Saccharomyces cerevisiae
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4.2.1.11
2-phospho-D-glycerate
-
680944
Saccharomyces cerevisiae
phosphoenolpyruvate + H2O
-
-
-
r
4.2.1.11
2-phospho-D-glycerate
direct transfer mechanisms of substrates between enolase and phosphoglycerate mutase predicted by molecular dynamics simulation
680944
Saccharomyces cerevisiae
phosphoenolpyruvate + H2O
-
-
-
r
Subunits
EC Number
Subunits
Commentary
Organism
5.4.2.11
More
molecular dynamics simulation reveals that the enzyme interacts with its C-terminal domain with enolase, suggesting a direct transfer mechanism of substrate
Saccharomyces cerevisiae
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
4.2.1.11
additional information
complex formation between active centers of enolase and phosphoglycerate mutase determined, interaction of enolase with C-terminal tail of phosphoglycerate mutase confirmed
Saccharomyces cerevisiae
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
4.2.1.11
additional information
complex formation between active centers of enolase and phosphoglycerate mutase determined, interaction of enolase with C-terminal tail of phosphoglycerate mutase confirmed
Saccharomyces cerevisiae
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
4.2.1.11
2-phospho-D-glycerate
Saccharomyces cerevisiae
-
phosphoenolpyruvate + H2O
-
-
r
Specific Activity [micromol/min/mg] (protein specific)
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
4.2.1.11
additional information
-
binding affinity between enolase and phosphoglycerate mutase confirmed by interaction energies and conformation changes, 10 A resolution and three orientations positioning enolase towards to phosphoglycerate mutase tested in presence of 150 mM NaCl
Saccharomyces cerevisiae
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4.2.1.11
2-phospho-D-glycerate
-
680944
Saccharomyces cerevisiae
phosphoenolpyruvate + H2O
-
-
-
r
4.2.1.11
2-phospho-D-glycerate
direct transfer mechanisms of substrates between enolase and phosphoglycerate mutase predicted by molecular dynamics simulation
680944
Saccharomyces cerevisiae
phosphoenolpyruvate + H2O
-
-
-
r
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
5.4.2.11
More
molecular dynamics simulation reveals that the enzyme interacts with its C-terminal domain with enolase, suggesting a direct transfer mechanism of substrate
Saccharomyces cerevisiae